ID A0A2G5TVR9_9PELO Unreviewed; 511 AA.
AC A0A2G5TVR9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 03-MAY-2023, entry version 14.
DE RecName: Full=Glucosylceramidase {ECO:0000256|ARBA:ARBA00012658, ECO:0000256|RuleBase:RU361188};
DE EC=3.2.1.45 {ECO:0000256|ARBA:ARBA00012658, ECO:0000256|RuleBase:RU361188};
GN Name=Cni-gba-3 {ECO:0000313|EMBL:PIC31201.1};
GN Synonyms=Cnig_chr_IV.g11974 {ECO:0000313|EMBL:PIC31201.1};
GN ORFNames=B9Z55_011974 {ECO:0000313|EMBL:PIC31201.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC31201.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-
CC acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269,
CC ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801,
CC ChEBI:CHEBI:52639; EC=3.2.1.45;
CC Evidence={ECO:0000256|RuleBase:RU361188};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family.
CC {ECO:0000256|ARBA:ARBA00005382, ECO:0000256|RuleBase:RU361188}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC31201.1}.
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DR EMBL; PDUG01000004; PIC31201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5TVR9; -.
DR Proteomes; UP000230233; Chromosome iv.
DR GO; GO:0004348; F:glucosylceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR033452; GH30_C.
DR InterPro; IPR001139; Glyco_hydro_30.
DR InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11069; GLUCOSYLCERAMIDASE; 1.
DR PANTHER; PTHR11069:SF41; GLUCOSYLCERAMIDASE 3-RELATED; 1.
DR Pfam; PF02055; Glyco_hydro_30; 1.
DR Pfam; PF17189; Glyco_hydro_30C; 1.
DR PRINTS; PR00843; GLHYDRLASE30.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361188};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361188};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361188};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sphingolipid metabolism {ECO:0000256|RuleBase:RU361188}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..511
FT /note="Glucosylceramidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013969422"
FT DOMAIN 103..439
FT /note="Glycosyl hydrolase family 30 TIM-barrel"
FT /evidence="ECO:0000259|Pfam:PF02055"
FT DOMAIN 442..505
FT /note="Glycosyl hydrolase family 30 beta sandwich"
FT /evidence="ECO:0000259|Pfam:PF17189"
SQ SEQUENCE 511 AA; 57425 MW; 2A8545D4301263F4 CRC64;
MREWKEIIWI LSVFVCSVRS SPCNSKIYDG AFKNLVCVCN ATSCDEIEPI GEIGDGKAVV
YRSTLDGDRL KRMSMKMGQK LGKDEVVNVT ISIDASERFQ QIFGFGGAFT DSAGEQLFAV
SEKVQEQIIN AYFGENGLEY NVGRVPIASC DFSTHEYSYD DVGEDFELKH FGLAEEDLKL
KKTKGKLQLF ASPWSAPGWM KTTGRMRGGG AMRNDKRVYE AYANYFIKFF EAYSSHSIPF
WGLTIQNEPS TGADMTWRWQ TMNYTAETMR DFLKDYLGPK LKGNKLTESL KVMILDDGRG
LLPGWADTIF NDTESTKYAD GIAVHWYGNL YSPAVLLDIT QRHHPDKFIF GTEACAGYFG
HHGPIMGDWF RAESYADDIL TDLNHHVTGW TDWNLCLDET GGPNWAYNVV DAPIIVNRTA
QEFYKQPMFY ALGHFSKFLP RGSTRVFTKV DGNLAVSAVS VVIEGGQRAT VILSKSSNSL
LTRVVDSATG YSLVLTLPPR SIHTIIWNKR K
//
